Over the last several decades, self-assembly has become a viable approach to create nanostructures by allowing control over feature size and organization at the molecular and mesoscopic length scales1,2. In organisms, proteins often display exquisite self-assembly3-5 through molecular recognition6, determined by their rich chemistry and wide range of conformations. Proteins also control solid interfaces in hard tissues, e.g., bones, spicules, shells, and teeth7-9, where they initiate nucleation or regulate specific mineral growth to form intricate solid structures10-12. It is, therefore, desirable to use proteins as molecular building blocks to control practical bio-solid interfaces. Earlier studies have used proteins to form organized nanostructures on solid surfaces, e.g., assembly of bacterial surface-layer proteins13, amyloids14,15, and de novo designed peptides on practical solids16,17. As in all protein self-assembly24, molecular recognition of solids must be governed by specific, non-covalent, interactions inherent in their sequence21,22,25. Correlation between primary amino acid sequences and their molecular interactions that lead to self-assembly on solid surfaces has not been established due to the complexities of protein/solid systems. Therefore, there have been no universal method to create proteins/peptides which can self-assemble into long-range ordered nanostructures or confluent ordered film on various materials. Furthermore, the interaction of ordered proteins or peptides with nano-materials has been unrevealed and uncontrolled. Still further, there have been no peptides found to form long-range ordered structures on graphene, the single atomic layer of graphite, or other atomic single layer materials.